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  • Ultrastructure  (3)
  • Springer  (3)
  • American Society of Hematology
  • Deutsches GeoForschungsZentrum GFZ
  • Oxford University Press
  • 2005-2009
  • 2000-2004
  • 1980-1984  (3)
  • 1960-1964
Collection
Publisher
  • Springer  (3)
  • American Society of Hematology
  • Deutsches GeoForschungsZentrum GFZ
  • Oxford University Press
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Year
  • 1
    ISSN: 1432-072X
    Keywords: Nitrobacter hamburgensis ; Nitrite oxidoreductase ; Nitrate reductase ; Molybdenum iron-sulfur protein ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nitrite oxidoreductase, the essential enzyme complex of nitrite oxidizing membranes, was isolated from cells of the nitrifying bacterium Nitrobacter hamburgensis. The enzyme system was solubilized and purified in the presence of 0.25% sodium deoxycholate. Nitrite oxidoreductase oxidized nitrite to nitrate in the presence of ferricyanide. The pH optimum was 8.0, and the apparent K m value for nitrite amounted to 3.6 mM. With reduced methyl-and benzylviologen nitrite oxidoreductase exhibited nitrate reductase activity with an apparent K m value of 0.9 mM for nitrate. NADH was also a suitable electron donor for nitrate reduction. The pH optimum was 7.0. Treatment with SDS resulted in the dissociation into 3 subunits of 116,000, 65,000 and 32,000. The enzyme complex contained iron, molydbenum, sulfur and copper. A c-type cytochrome was present. Isolated nitrite oxidoreductase is a particle of 95±30 Å in diameter.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 216 (1981), S. 491-501 
    ISSN: 1432-0878
    Keywords: Ultrastructure ; Cornea ; Compound eye ; Honey bee (Apis mellifera)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The fine structure of the cornea in an anatomically and functionally specialized part of the honey bee's compound eye (dorsal rim area) was examined by light microscopy, transmission electron and scanning electron microscopy. Under incident illumination the cornea appears grey and cloudy, leaving only the centers of the corneal lenses clear. This is due to numerous pore canals that penetrate the cornea from the inside, ending a few μm below the outer surface. They consist of (1) a small cylindrical cellular evagination of a pigment cell (proximal), and (2) a rugged-walled, pinetree-shaped extracellular part (distal). The functional significance of these pore canals is discussed. It is concluded that their light scattering properties cause the wide visual fields of the photoreceptor cells measured electrophysiologically in the dorsal rim area, and that this is related to the way this eye region detects polarization in skylight.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0878
    Keywords: UV-irradiation ; Compound eye Rhabdomeres ; Trophospongium ; Ultrastructure ; Lepidoptera, Insecta
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Presumably, as a consequence of a 3-h exposure to light of 350-nm wavelength (1.5 × 1015 photons/cm2 sec) followed by a period of 20 h of rest in the dark, the four smaller retinula cells in each ommatidium of the eye of the butterfly Papilio xuthus contain a structure in the peripheral regions of their cytoplasm that resembles a portion of a rhabdom. Evidence for and against the view that this unusual, highly ordered arrangement of membranes represents a trophospongium is presented. In view of the fact that the structure in question only occurred at the same time when rhabdomeres were in a process of disintegration or reformation, the authors conclude that the structure in question is involved in the supply or removal of substances during a period of considerable activity of the retinula cell.
    Type of Medium: Electronic Resource
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